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Toxicon ; 83: 15-21, 2014 Jun.
Article in English | MEDLINE | ID: mdl-24560880

ABSTRACT

Mature Ts1, the main neurotoxin from Tityus serrulatus venom, has its C-terminal Cys amidated, while the isolated isoform of Ts1, named Ts1-G, keeps the non-amidated Gly residue at the C-terminal region, allowing the study of the comparative functional importance of amidation at the C-terminal between these two native toxins. Voltage dependent sodium current measurements showed that the affinity of Ts1-G for sodium channels is smaller than that of the mature Ts1, confirming the important role played by the C-terminal amidation in determining Ts1 activity.


Subject(s)
Arthropod Proteins/chemistry , Insect Proteins/chemistry , Neurotoxins/chemistry , Scorpion Venoms/chemistry , Amino Acid Sequence , Animals , Arthropod Proteins/isolation & purification , Arthropod Proteins/toxicity , Blood Glucose/drug effects , Chemical Fractionation , Insect Proteins/isolation & purification , Insect Proteins/toxicity , Male , Mice, Inbred Strains , Molecular Sequence Data , Neurotoxins/isolation & purification , Neurotoxins/toxicity , Protein Isoforms/chemistry , Protein Isoforms/isolation & purification , Protein Isoforms/toxicity , Scorpion Venoms/isolation & purification , Scorpion Venoms/toxicity , Scorpions , Sequence Alignment
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